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Interaction between Galectin-3 and Integrins Mediates Cell-Matrix Adhesion in Endothelial Cells and Mesenchymal Stem Cells
- 1.0543839 - FGÚ 2022 RIV CH eng J - Journal Article
Sedlář, Antonín - Trávníčková, Martina - Bojarová, Pavla - Vlachová, Miluše - Slámová, Kristýna - Křen, Vladimír - Bačáková, Lucie
Interaction between Galectin-3 and Integrins Mediates Cell-Matrix Adhesion in Endothelial Cells and Mesenchymal Stem Cells.
International Journal of Molecular Sciences. Roč. 22, č. 10 (2021), č. článku 5144. E-ISSN 1422-0067
R&D Projects: GA MŠk(CZ) LM2018129; GA MŠk(CZ) EF18_046/0016045; GA ČR(CZ) GA18-01163S; GA MŠk(CZ) LTC18041; GA MŠk(CZ) LTC18038
Institutional support: RVO:67985823 ; RVO:61388971
Keywords : galectin * HUVEC * ADSC * integrin * carbohydrate
OECD category: Biomaterials (as related to medical implants, devices, sensors); Biomaterials (as related to medical implants, devices, sensors) (MBU-M)
Impact factor: 6.208, year: 2021
Method of publishing: Open access
Galectin-3 (Gal-3) is a beta-galactoside-binding protein that influences various cell functions, including cell adhesion. We focused on the role of Gal-3 as an extracellular ligand mediating cell-matrix adhesion. We used human adipose tissue-derived stem cells and human umbilical vein endothelial cells that are promising for vascular tissue engineering. We found that these cells naturally contained Gal-3 on their surface and inside the cells. Moreover, they were able to associate with exogenous Gal-3 added to the culture medium. This association was reduced with a beta-galactoside LacdiNAc (GalNAc beta 1,4GlcNAc), a selective ligand of Gal-3, which binds to the carbohydrate recognition domain (CRD) in the Gal-3 molecule. This ligand was also able to detach Gal-3 newly associated with cells but not Gal-3 naturally present on cells. In addition, Gal-3 preadsorbed on plastic surfaces acted as an adhesion ligand for both cell types, and the cell adhesion was resistant to blocking with LacdiNAc. This result suggests that the adhesion was mediated by a binding site different from the CRD. The blocking of integrin adhesion receptors on cells with specific antibodies revealed that the cell adhesion to the preadsorbed Gal-3 was mediated, at least partially, by beta 1 and alpha V integrins-namely alpha 5 beta 1, alpha V beta 3, and alpha V beta 1 integrins.
Permanent Link: http://hdl.handle.net/11104/0320954
Number of the records: 1